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Metal Ion Chaperone Function of the Soluble Cu(I) Receptor Atx1

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Science  31 Oct 1997:
Vol. 278, Issue 5339, pp. 853-856
DOI: 10.1126/science.278.5339.853

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Abstract

Reactive and potentially toxic cofactors such as copper ions are imported into eukaryotic cells and incorporated into target proteins by unknown mechanisms. Atx1, a prototypical copper chaperone protein from yeast, has now been shown to act as a soluble cytoplasmic copper(I) receptor that can adopt either a two- or three-coordinate metal center in the active site. Atx1 also associated directly with the Atx1-like cytosolic domains of Ccc2, a vesicular protein defined in genetic studies as a member of the copper-trafficking pathway. The unusual structure and dynamics of Atx1 suggest a copper exchange function for this protein and related domains in the Menkes and Wilson disease proteins.

  • * To whom correspondence should be addressed. E-mail: t-ohalloran{at}nwu.edu

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